EBP_HUMAN
ID EBP_HUMAN Reviewed; 230 AA.
AC Q15125; Q6FGL3; Q6IBI9;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=3-beta-hydroxysteroid-Delta(8),Delta(7)-isomerase {ECO:0000305};
DE EC=5.3.3.5 {ECO:0000269|PubMed:12760743, ECO:0000269|PubMed:8798407, ECO:0000269|PubMed:9894009};
DE AltName: Full=Cholestenol Delta-isomerase;
DE AltName: Full=Delta(8)-Delta(7) sterol isomerase;
DE Short=D8-D7 sterol isomerase;
DE AltName: Full=Emopamil-binding protein;
GN Name=EBP {ECO:0000312|HGNC:HGNC:3133};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=7706302; DOI=10.1074/jbc.270.13.7551;
RA Hanner M., Moebius F.F., Weber F., Grabner M., Striessnig J., Glossmann H.;
RT "Phenylalkylamine Ca2+ antagonist binding protein. Molecular cloning,
RT tissue distribution, and heterologous expression.";
RL J. Biol. Chem. 270:7551-7557(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Cervix, and Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP CATALYTIC ACTIVITY, FUNCTION, AND PATHWAY.
RX PubMed=8798407; DOI=10.1074/jbc.271.37.22434;
RA Silve S., Dupuy P.H., Labit-Lebouteiller C., Kaghad M., Chalon P.,
RA Rahier A., Taton M., Lupker J., Shire D., Loison G.;
RT "Emopamil-binding protein, a mammalian protein that binds a series of
RT structurally diverse neuroprotective agents, exhibits delta8-delta7 sterol
RT isomerase activity in yeast.";
RL J. Biol. Chem. 271:22434-22440(1996).
RN [7]
RP CATALYTIC ACTIVITY, FUNCTION, PATHWAY, AND MUTAGENESIS.
RX PubMed=9894009; DOI=10.1021/bi981804i;
RA Moebius F.F., Soellner K.E.M., Fiechtner B., Huck C.W., Bonn G.,
RA Glossmann H.;
RT "Histidine77, glutamic acid81, glutamic acid123, threonine126,
RT asparagine194, and tryptophan197 of the human emopamil binding protein are
RT required for in vivo sterol delta 8-delta 7 isomerization.";
RL Biochemistry 38:1119-1127(1999).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=10406945; DOI=10.1046/j.1432-1327.1999.00500.x;
RA Dussossoy D., Carayon P., Belugou S., Feraut D., Bord A., Goubet C.,
RA Roque C., Vidal H., Combes T., Loison G., Casellas P.;
RT "Colocalization of sterol isomerase and sigma(1) receptor at endoplasmic
RT reticulum and nuclear envelope level.";
RL Eur. J. Biochem. 263:377-386(1999).
RN [9]
RP INVOLVEMENT IN MEND, VARIANT MEND PRO-18, AND CHARACTERIZATION OF VARIANT
RP MEND PRO-18.
RX PubMed=12503101; DOI=10.1002/ajmg.a.10849;
RA Milunsky J.M., Maher T.A., Metzenberg A.B.;
RT "Molecular, biochemical, and phenotypic analysis of a hemizygous male with
RT a severe atypical phenotype for X-linked dominant Conradi-Hunermann-Happle
RT syndrome and a mutation in EBP.";
RL Am. J. Med. Genet. A 116A:249-254(2003).
RN [10]
RP CATALYTIC ACTIVITY, FUNCTION, PATHWAY, AND MUTAGENESIS OF TYR-111; MET-121
RP AND PHE-189.
RX PubMed=12760743; DOI=10.1042/bj20030465;
RA Moebius F.F., Fitzky B.U., Wietzorrek G., Haidekker A., Eder A.,
RA Glossmann H.;
RT "Cloning of an emopamil-binding protein (EBP)-like protein that lacks
RT sterol delta8-delta7 isomerase activity.";
RL Biochem. J. 374:229-237(2003).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [12]
RP INVOLVEMENT IN MEND, VARIANT MEND CYS-47, AND CHARACTERIZATION OF VARIANT
RP MEND CYS-47.
RX PubMed=20949533; DOI=10.1002/ajmg.a.33674;
RA Furtado L.V., Bayrak-Toydemir P., Hulinsky B., Damjanovich K., Carey J.C.,
RA Rope A.F.;
RT "A novel X-linked multiple congenital anomaly syndrome associated with an
RT EBP mutation.";
RL Am. J. Med. Genet. A 152A:2838-2844(2010).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [15]
RP VARIANT CDPX2 GLN-110.
RX PubMed=10391218; DOI=10.1038/10350;
RA Derry J.M.J., Gormally E., Means G.D., Zhao W., Meindl A., Kelley R.I.,
RA Boyd Y., Herman G.E.;
RT "Mutations in a delta(8)-delta(7) sterol isomerase in the tattered mouse
RT and X-linked dominant chondrodysplasia punctata.";
RL Nat. Genet. 22:286-290(1999).
RN [16]
RP VARIANTS CDPX2 LYS-80 AND HIS-147.
RX PubMed=10391219; DOI=10.1038/10357;
RA Braverman N., Lin P., Moebius F.F., Obie C., Moser A., Glossmann H.,
RA Wilcox W.R., Rimoin D.L., Smith M., Kratz L., Kelley R.I., Valle D.;
RT "Mutations in the gene encoding 3-beta-hydroxysteroid-delta(8),delta(7)-
RT isomerase cause X-linked dominant Conradi-Hunermann syndrome.";
RL Nat. Genet. 22:291-294(1999).
RN [17]
RP VARIANT CDPX2 HIS-147.
RX PubMed=10942423; DOI=10.1093/hmg/9.13.1951;
RA Has C., Bruckner-Tuderman L., Muller D., Floeth M., Folkers E., Donnai D.,
RA Traupe H.;
RT "The Conradi-Hunermann-Happle syndrome (CDPX2) and emopamil binding
RT protein: novel mutations, and somatic and gonadal mosaicism.";
RL Hum. Mol. Genet. 9:1951-1955(2000).
RN [18]
RP VARIANT CDPX2 GLY-147.
RX PubMed=11493318; DOI=10.1034/j.1600-0625.2001.100409.x;
RA Becker K., Csikos M., Horvath A., Karpati S.;
RT "Identification of a novel mutation in 3beta-hydroxysteroid-Delta8-Delta7-
RT isomerase in a case of Conradi-Hunermann-Happle syndrome.";
RL Exp. Dermatol. 10:286-289(2001).
RN [19]
RP VARIANT CDPX2 LYS-103.
RX PubMed=18176751; DOI=10.2340/00015555-0337;
RA Kolb-Maeurer A., Grzeschik K.H., Haas D., Broecker E.B., Hamm H.;
RT "Conradi-Huenermann-Happle syndrome (X-linked dominant chondrodysplasia
RT punctata) confirmed by plasma sterol and mutation analysis.";
RL Acta Derm. Venereol. 88:47-51(2008).
RN [20]
RP VARIANT MEND ARG-47, AND CHARACTERIZATION OF VARIANT MEND ARG-47.
RX PubMed=24459067; DOI=10.1002/ajmg.a.36368;
RA Hartill V.L., Tysoe C., Manning N., Dobbie A., Santra S., Walter J.,
RA Caswell R., Koster J., Waterham H., Hobson E.;
RT "An unusual phenotype of X-linked developmental delay and extreme
RT behavioral difficulties associated with a mutation in the EBP gene.";
RL Am. J. Med. Genet. A 164A:907-914(2014).
RN [21]
RP VARIANT MEND ASN-75, AND CHARACTERIZATION OF VARIANT MEND ASN-75.
RX PubMed=24700572; DOI=10.1002/ajmg.a.36508;
RA Barboza-Cerda M.C., Wong L.J., Martinez-de-Villarreal L.E., Zhang V.W.,
RA Dector M.A.;
RT "A novel EBP c.224T>A mutation supports the existence of a male-specific
RT disorder independent of CDPX2.";
RL Am. J. Med. Genet. A 164A:1642-1647(2014).
RN [22]
RP VARIANT CDPX2 HIS-147.
RX PubMed=25814754; DOI=10.4103/0019-5154.152570;
RA Ozyurt K., Subasioglu A., Ozturk P., Inci R., Ozkan F., Bueno E.,
RA Canueto J., Gonzalez Sarmiento R.;
RT "Emopamil binding protein mutation in conradi-huenermann-happle syndrome
RT representing plaque-type psoriasis.";
RL Indian J. Dermatol. 60:216-216(2015).
CC -!- FUNCTION: Catalyzes the conversion of Delta(8)-sterols to their
CC corresponding Delta(7)-isomers. {ECO:0000269|PubMed:12760743,
CC ECO:0000269|PubMed:8798407, ECO:0000269|PubMed:9894009}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=lathosterol = 5alpha-cholest-8-en-3beta-ol;
CC Xref=Rhea:RHEA:15281, ChEBI:CHEBI:16608, ChEBI:CHEBI:17168;
CC EC=5.3.3.5; Evidence={ECO:0000269|PubMed:12760743,
CC ECO:0000269|PubMed:8798407, ECO:0000269|PubMed:9894009};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15282;
CC Evidence={ECO:0000305|PubMed:12760743, ECO:0000305|PubMed:8798407,
CC ECO:0000305|PubMed:9894009};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=zymosterol = 5alpha-cholesta-7,24-dien-3beta-ol;
CC Xref=Rhea:RHEA:33999, ChEBI:CHEBI:16290, ChEBI:CHEBI:18252;
CC Evidence={ECO:0000269|PubMed:8798407, ECO:0000269|PubMed:9894009};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:34000;
CC Evidence={ECO:0000305|PubMed:8798407, ECO:0000305|PubMed:9894009};
CC -!- PATHWAY: Steroid biosynthesis; cholesterol biosynthesis.
CC {ECO:0000269|PubMed:12760743, ECO:0000269|PubMed:8798407,
CC ECO:0000269|PubMed:9894009}.
CC -!- INTERACTION:
CC Q15125; O95870: ABHD16A; NbExp=3; IntAct=EBI-3915253, EBI-348517;
CC Q15125; Q86W74-2: ANKRD46; NbExp=3; IntAct=EBI-3915253, EBI-12109402;
CC Q15125; Q13520: AQP6; NbExp=3; IntAct=EBI-3915253, EBI-13059134;
CC Q15125; Q3SXY8: ARL13B; NbExp=3; IntAct=EBI-3915253, EBI-11343438;
CC Q15125; Q8N6S5: ARL6IP6; NbExp=3; IntAct=EBI-3915253, EBI-2808844;
CC Q15125; Q9H2C2: ARV1; NbExp=3; IntAct=EBI-3915253, EBI-11724186;
CC Q15125; Q9HD20-3: ATP13A1; NbExp=3; IntAct=EBI-3915253, EBI-12069500;
CC Q15125; O95393: BMP10; NbExp=3; IntAct=EBI-3915253, EBI-3922513;
CC Q15125; Q12983: BNIP3; NbExp=3; IntAct=EBI-3915253, EBI-749464;
CC Q15125; Q8WVV5: BTN2A2; NbExp=3; IntAct=EBI-3915253, EBI-8648738;
CC Q15125; P06681: C2; NbExp=3; IntAct=EBI-3915253, EBI-2835920;
CC Q15125; O14523: C2CD2L; NbExp=3; IntAct=EBI-3915253, EBI-12822627;
CC Q15125; Q8WVX3-2: C4orf3; NbExp=3; IntAct=EBI-3915253, EBI-12003442;
CC Q15125; P01031: C5; NbExp=3; IntAct=EBI-3915253, EBI-8558308;
CC Q15125; Q6UWT4: C5orf46; NbExp=3; IntAct=EBI-3915253, EBI-11986083;
CC Q15125; Q9P0B6: CCDC167; NbExp=3; IntAct=EBI-3915253, EBI-9083477;
CC Q15125; Q8NHW4: CCL4L2; NbExp=3; IntAct=EBI-3915253, EBI-10271156;
CC Q15125; P25942: CD40; NbExp=3; IntAct=EBI-3915253, EBI-525714;
CC Q15125; Q07108: CD69; NbExp=3; IntAct=EBI-3915253, EBI-2836595;
CC Q15125; P60033: CD81; NbExp=3; IntAct=EBI-3915253, EBI-712921;
CC Q15125; O14735: CDIPT; NbExp=3; IntAct=EBI-3915253, EBI-358858;
CC Q15125; P23141-3: CES1; NbExp=3; IntAct=EBI-3915253, EBI-12360993;
CC Q15125; Q9H9P2: CHODL; NbExp=3; IntAct=EBI-3915253, EBI-17447707;
CC Q15125; Q8NHS1: CLDND2; NbExp=3; IntAct=EBI-3915253, EBI-11959453;
CC Q15125; O43889-2: CREB3; NbExp=3; IntAct=EBI-3915253, EBI-625022;
CC Q15125; Q96BA8: CREB3L1; NbExp=5; IntAct=EBI-3915253, EBI-6942903;
CC Q15125; P49447: CYB561; NbExp=3; IntAct=EBI-3915253, EBI-8646596;
CC Q15125; O43169: CYB5B; NbExp=3; IntAct=EBI-3915253, EBI-1058710;
CC Q15125; P78329: CYP4F2; NbExp=3; IntAct=EBI-3915253, EBI-1752413;
CC Q15125; P81534: DEFB103B; NbExp=3; IntAct=EBI-3915253, EBI-12074168;
CC Q15125; Q9H1M4: DEFB127; NbExp=3; IntAct=EBI-3915253, EBI-10305240;
CC Q15125; Q96LL9: DNAJC30; NbExp=3; IntAct=EBI-3915253, EBI-8639143;
CC Q15125; Q15125: EBP; NbExp=3; IntAct=EBI-3915253, EBI-3915253;
CC Q15125; Q08426: EHHADH; NbExp=3; IntAct=EBI-3915253, EBI-2339219;
CC Q15125; Q9BV81: EMC6; NbExp=3; IntAct=EBI-3915253, EBI-2820492;
CC Q15125; P54849: EMP1; NbExp=3; IntAct=EBI-3915253, EBI-4319440;
CC Q15125; Q9UKR5: ERG28; NbExp=3; IntAct=EBI-3915253, EBI-711490;
CC Q15125; Q9Y282: ERGIC3; NbExp=3; IntAct=EBI-3915253, EBI-781551;
CC Q15125; Q7L5A8: FA2H; NbExp=3; IntAct=EBI-3915253, EBI-11337888;
CC Q15125; Q5JX71: FAM209A; NbExp=3; IntAct=EBI-3915253, EBI-18304435;
CC Q15125; Q96IV6: FAXDC2; NbExp=3; IntAct=EBI-3915253, EBI-12142299;
CC Q15125; Q9UGM5: FETUB; NbExp=3; IntAct=EBI-3915253, EBI-13049494;
CC Q15125; Q9Y3D6: FIS1; NbExp=3; IntAct=EBI-3915253, EBI-3385283;
CC Q15125; Q14318: FKBP8; NbExp=3; IntAct=EBI-3915253, EBI-724839;
CC Q15125; Q9BWH2: FUNDC2; NbExp=3; IntAct=EBI-3915253, EBI-714482;
CC Q15125; Q14802-3: FXYD3; NbExp=3; IntAct=EBI-3915253, EBI-12175685;
CC Q15125; Q9H0Q3: FXYD6; NbExp=3; IntAct=EBI-3915253, EBI-713304;
CC Q15125; Q8WWP7: GIMAP1; NbExp=3; IntAct=EBI-3915253, EBI-11991950;
CC Q15125; Q96F15: GIMAP5; NbExp=3; IntAct=EBI-3915253, EBI-6166686;
CC Q15125; P29033: GJB2; NbExp=3; IntAct=EBI-3915253, EBI-3905204;
CC Q15125; O95452: GJB6; NbExp=3; IntAct=EBI-3915253, EBI-13345609;
CC Q15125; O14653: GOSR2; NbExp=3; IntAct=EBI-3915253, EBI-4401517;
CC Q15125; Q8TDT2: GPR152; NbExp=3; IntAct=EBI-3915253, EBI-13345167;
CC Q15125; P02724: GYPA; NbExp=3; IntAct=EBI-3915253, EBI-702665;
CC Q15125; P30519: HMOX2; NbExp=3; IntAct=EBI-3915253, EBI-712096;
CC Q15125; Q7Z5P4: HSD17B13; NbExp=3; IntAct=EBI-3915253, EBI-18053395;
CC Q15125; Q9Y5U9: IER3IP1; NbExp=3; IntAct=EBI-3915253, EBI-725665;
CC Q15125; Q9Y5U4: INSIG2; NbExp=3; IntAct=EBI-3915253, EBI-8503746;
CC Q15125; Q8N5M9: JAGN1; NbExp=3; IntAct=EBI-3915253, EBI-10266796;
CC Q15125; Q5T700: LDLRAD1; NbExp=3; IntAct=EBI-3915253, EBI-10173166;
CC Q15125; Q68G75: LEMD1; NbExp=3; IntAct=EBI-3915253, EBI-12268900;
CC Q15125; Q7L5N7: LPCAT2; NbExp=3; IntAct=EBI-3915253, EBI-4280011;
CC Q15125; Q7Z4F1: LRP10; NbExp=3; IntAct=EBI-3915253, EBI-2830349;
CC Q15125; Q96AG4: LRRC59; NbExp=3; IntAct=EBI-3915253, EBI-358888;
CC Q15125; Q16873: LTC4S; NbExp=3; IntAct=EBI-3915253, EBI-12241118;
CC Q15125; Q6ZSS7: MFSD6; NbExp=3; IntAct=EBI-3915253, EBI-2858252;
CC Q15125; P50281: MMP14; NbExp=3; IntAct=EBI-3915253, EBI-992788;
CC Q15125; Q5J8X5: MS4A13; NbExp=3; IntAct=EBI-3915253, EBI-12070086;
CC Q15125; Q9UHE5: NAT8; NbExp=3; IntAct=EBI-3915253, EBI-2863634;
CC Q15125; O95167: NDUFA3; NbExp=3; IntAct=EBI-3915253, EBI-1246131;
CC Q15125; Q9NX14: NDUFB11; NbExp=3; IntAct=EBI-3915253, EBI-1246182;
CC Q15125; Q99519: NEU1; NbExp=3; IntAct=EBI-3915253, EBI-721517;
CC Q15125; Q92982: NINJ1; NbExp=3; IntAct=EBI-3915253, EBI-2802124;
CC Q15125; Q9NZG7: NINJ2; NbExp=3; IntAct=EBI-3915253, EBI-10317425;
CC Q15125; Q16617: NKG7; NbExp=3; IntAct=EBI-3915253, EBI-3919611;
CC Q15125; Q8IXM6: NRM; NbExp=3; IntAct=EBI-3915253, EBI-10262547;
CC Q15125; Q2M2E3: ODF4; NbExp=3; IntAct=EBI-3915253, EBI-12382569;
CC Q15125; Q9P0S3: ORMDL1; NbExp=3; IntAct=EBI-3915253, EBI-1054848;
CC Q15125; Q53FV1: ORMDL2; NbExp=3; IntAct=EBI-3915253, EBI-11075081;
CC Q15125; Q8N138: ORMDL3; NbExp=3; IntAct=EBI-3915253, EBI-721750;
CC Q15125; Q7RTS5: OTOP3; NbExp=3; IntAct=EBI-3915253, EBI-12853910;
CC Q15125; Q9Y342: PLLP; NbExp=3; IntAct=EBI-3915253, EBI-3919291;
CC Q15125; Q04941: PLP2; NbExp=3; IntAct=EBI-3915253, EBI-608347;
CC Q15125; Q8IY26: PLPP6; NbExp=3; IntAct=EBI-3915253, EBI-11721828;
CC Q15125; Q01453: PMP22; NbExp=3; IntAct=EBI-3915253, EBI-2845982;
CC Q15125; P54315: PNLIPRP1; NbExp=3; IntAct=EBI-3915253, EBI-8652812;
CC Q15125; P43378: PTPN9; NbExp=3; IntAct=EBI-3915253, EBI-742898;
CC Q15125; P15151: PVR; NbExp=3; IntAct=EBI-3915253, EBI-3919694;
CC Q15125; Q8N8N0: RNF152; NbExp=3; IntAct=EBI-3915253, EBI-2129725;
CC Q15125; Q5QGT7: RTP2; NbExp=3; IntAct=EBI-3915253, EBI-10244780;
CC Q15125; Q96GQ5: RUSF1; NbExp=3; IntAct=EBI-3915253, EBI-8636004;
CC Q15125; Q9NTJ5: SACM1L; NbExp=3; IntAct=EBI-3915253, EBI-3917235;
CC Q15125; Q969E2: SCAMP4; NbExp=3; IntAct=EBI-3915253, EBI-4403649;
CC Q15125; O75396: SEC22B; NbExp=3; IntAct=EBI-3915253, EBI-1058865;
CC Q15125; Q9Y6X1: SERP1; NbExp=3; IntAct=EBI-3915253, EBI-10329948;
CC Q15125; Q8N6R1: SERP2; NbExp=3; IntAct=EBI-3915253, EBI-749270;
CC Q15125; A0A1P0AYU5: SFXN3; NbExp=3; IntAct=EBI-3915253, EBI-14193895;
CC Q15125; Q8TD22: SFXN5; NbExp=3; IntAct=EBI-3915253, EBI-17274136;
CC Q15125; Q8IWU4: SLC30A8; NbExp=3; IntAct=EBI-3915253, EBI-10262251;
CC Q15125; Q96G79: SLC35A4; NbExp=3; IntAct=EBI-3915253, EBI-12363689;
CC Q15125; Q2M3R5: SLC35G1; NbExp=3; IntAct=EBI-3915253, EBI-13311257;
CC Q15125; Q9NVC3: SLC38A7; NbExp=3; IntAct=EBI-3915253, EBI-10314552;
CC Q15125; P08195-4: SLC3A2; NbExp=3; IntAct=EBI-3915253, EBI-12832276;
CC Q15125; Q96JW4: SLC41A2; NbExp=3; IntAct=EBI-3915253, EBI-10290130;
CC Q15125; Q6P1K1: SLC48A1; NbExp=3; IntAct=EBI-3915253, EBI-1222191;
CC Q15125; Q0VAQ4: SMAGP; NbExp=3; IntAct=EBI-3915253, EBI-10226799;
CC Q15125; Q9NRQ5: SMCO4; NbExp=3; IntAct=EBI-3915253, EBI-8640191;
CC Q15125; B2RUZ4: SMIM1; NbExp=3; IntAct=EBI-3915253, EBI-12188413;
CC Q15125; Q9BZL3: SMIM3; NbExp=3; IntAct=EBI-3915253, EBI-741850;
CC Q15125; Q6UX34: SNORC; NbExp=3; IntAct=EBI-3915253, EBI-11957067;
CC Q15125; Q86Y82: STX12; NbExp=3; IntAct=EBI-3915253, EBI-2691717;
CC Q15125; P61266: STX1B; NbExp=3; IntAct=EBI-3915253, EBI-9071709;
CC Q15125; Q13190: STX5; NbExp=3; IntAct=EBI-3915253, EBI-714206;
CC Q15125; O43752: STX6; NbExp=3; IntAct=EBI-3915253, EBI-2695795;
CC Q15125; O15400: STX7; NbExp=3; IntAct=EBI-3915253, EBI-3221827;
CC Q15125; Q9UNK0: STX8; NbExp=3; IntAct=EBI-3915253, EBI-727240;
CC Q15125; O43759-2: SYNGR1; NbExp=3; IntAct=EBI-3915253, EBI-12187159;
CC Q15125; P57105: SYNJ2BP; NbExp=3; IntAct=EBI-3915253, EBI-1049004;
CC Q15125; Q8N2H4: SYS1; NbExp=3; IntAct=EBI-3915253, EBI-13075176;
CC Q15125; Q96BZ9: TBC1D20; NbExp=3; IntAct=EBI-3915253, EBI-9254454;
CC Q15125; P07204: THBD; NbExp=3; IntAct=EBI-3915253, EBI-941422;
CC Q15125; O14925: TIMM23; NbExp=3; IntAct=EBI-3915253, EBI-1047996;
CC Q15125; Q96CP7: TLCD1; NbExp=3; IntAct=EBI-3915253, EBI-11337932;
CC Q15125; Q96MV1: TLCD4; NbExp=3; IntAct=EBI-3915253, EBI-12947623;
CC Q15125; P55061: TMBIM6; NbExp=3; IntAct=EBI-3915253, EBI-1045825;
CC Q15125; Q9NV29: TMEM100; NbExp=3; IntAct=EBI-3915253, EBI-8644968;
CC Q15125; P17152: TMEM11; NbExp=3; IntAct=EBI-3915253, EBI-723946;
CC Q15125; Q9BXJ8: TMEM120A; NbExp=3; IntAct=EBI-3915253, EBI-727322;
CC Q15125; A0PK00: TMEM120B; NbExp=3; IntAct=EBI-3915253, EBI-10171534;
CC Q15125; Q9NV12: TMEM140; NbExp=3; IntAct=EBI-3915253, EBI-2844246;
CC Q15125; Q9BVK8: TMEM147; NbExp=3; IntAct=EBI-3915253, EBI-348587;
CC Q15125; Q9NUH8: TMEM14B; NbExp=3; IntAct=EBI-3915253, EBI-8638294;
CC Q15125; Q9P0S9: TMEM14C; NbExp=3; IntAct=EBI-3915253, EBI-2339195;
CC Q15125; Q9NRX6: TMEM167B; NbExp=3; IntAct=EBI-3915253, EBI-17684533;
CC Q15125; Q8N511: TMEM199; NbExp=3; IntAct=EBI-3915253, EBI-10265825;
CC Q15125; Q969S6: TMEM203; NbExp=3; IntAct=EBI-3915253, EBI-12274070;
CC Q15125; Q9BTX3: TMEM208; NbExp=3; IntAct=EBI-3915253, EBI-12876824;
CC Q15125; A2RU14: TMEM218; NbExp=3; IntAct=EBI-3915253, EBI-10173151;
CC Q15125; Q9H0R3: TMEM222; NbExp=3; IntAct=EBI-3915253, EBI-347385;
CC Q15125; Q8NBD8: TMEM229B; NbExp=3; IntAct=EBI-3915253, EBI-12195227;
CC Q15125; Q8WW34-2: TMEM239; NbExp=3; IntAct=EBI-3915253, EBI-11528917;
CC Q15125; Q9NWH2: TMEM242; NbExp=3; IntAct=EBI-3915253, EBI-10315004;
CC Q15125; Q9BU79: TMEM243; NbExp=3; IntAct=EBI-3915253, EBI-12887458;
CC Q15125; Q8TBM7: TMEM254; NbExp=3; IntAct=EBI-3915253, EBI-11956809;
CC Q15125; Q69YG0: TMEM42; NbExp=3; IntAct=EBI-3915253, EBI-12038591;
CC Q15125; Q9NW97: TMEM51; NbExp=3; IntAct=EBI-3915253, EBI-726044;
CC Q15125; Q9H2L4: TMEM60; NbExp=3; IntAct=EBI-3915253, EBI-2852148;
CC Q15125; Q6PI78: TMEM65; NbExp=3; IntAct=EBI-3915253, EBI-6656213;
CC Q15125; Q8N2M4: TMEM86A; NbExp=3; IntAct=EBI-3915253, EBI-12015604;
CC Q15125; Q8N661: TMEM86B; NbExp=3; IntAct=EBI-3915253, EBI-2548832;
CC Q15125; Q5BJF2: TMEM97; NbExp=3; IntAct=EBI-3915253, EBI-12111910;
CC Q15125; Q9NSU2-1: TREX1; NbExp=3; IntAct=EBI-3915253, EBI-16746122;
CC Q15125; A0AVG3: TSNARE1; NbExp=3; IntAct=EBI-3915253, EBI-12003468;
CC Q15125; Q5TGU0: TSPO2; NbExp=3; IntAct=EBI-3915253, EBI-12195249;
CC Q15125; A5PKU2: TUSC5; NbExp=3; IntAct=EBI-3915253, EBI-11988865;
CC Q15125; Q9Y385: UBE2J1; NbExp=3; IntAct=EBI-3915253, EBI-988826;
CC Q15125; Q9Y5Z9: UBIAD1; NbExp=3; IntAct=EBI-3915253, EBI-2819725;
CC Q15125; Q53HI1: UNC50; NbExp=3; IntAct=EBI-3915253, EBI-7601760;
CC Q15125; Q9H1C4: UNC93B1; NbExp=3; IntAct=EBI-3915253, EBI-4401271;
CC Q15125; Q9NZ43: USE1; NbExp=3; IntAct=EBI-3915253, EBI-742842;
CC Q15125; P23763-3: VAMP1; NbExp=3; IntAct=EBI-3915253, EBI-12097582;
CC Q15125; P63027: VAMP2; NbExp=3; IntAct=EBI-3915253, EBI-520113;
CC Q15125; Q15836: VAMP3; NbExp=3; IntAct=EBI-3915253, EBI-722343;
CC Q15125; O75379: VAMP4; NbExp=3; IntAct=EBI-3915253, EBI-744953;
CC Q15125; Q9P0L0: VAPA; NbExp=3; IntAct=EBI-3915253, EBI-1059156;
CC Q15125; O95292: VAPB; NbExp=3; IntAct=EBI-3915253, EBI-1188298;
CC Q15125; O95070: YIF1A; NbExp=3; IntAct=EBI-3915253, EBI-2799703;
CC Q15125; Q9Y548: YIPF1; NbExp=3; IntAct=EBI-3915253, EBI-7850136;
CC Q15125; Q9BSR8: YIPF4; NbExp=3; IntAct=EBI-3915253, EBI-751253;
CC Q15125; Q96EC8: YIPF6; NbExp=3; IntAct=EBI-3915253, EBI-751210;
CC Q15125; Q6UX98: ZDHHC24; NbExp=3; IntAct=EBI-3915253, EBI-10254561;
CC Q15125; O95159: ZFPL1; NbExp=3; IntAct=EBI-3915253, EBI-718439;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:10406945}; Multi-pass membrane protein
CC {ECO:0000305}. Nucleus envelope {ECO:0000269|PubMed:10406945}.
CC Cytoplasmic vesicle {ECO:0000269|PubMed:10406945}. Note=During
CC interphase, detected on the endoplasmic reticulum and the nuclear
CC envelope. During mitosis, detected on cytoplasmic vesicles.
CC {ECO:0000269|PubMed:10406945}.
CC -!- DISEASE: Chondrodysplasia punctata 2, X-linked dominant (CDPX2)
CC [MIM:302960]: A clinically and genetically heterogeneous disorder
CC characterized by punctiform calcification of the bones. The key
CC clinical features of CDPX2 are chondrodysplasia punctata, linear
CC ichthyosis, cataracts and short stature. CDPX2 is a rare disorder of
CC defective cholesterol biosynthesis, biochemically characterized by an
CC increased amount of 8-dehydrocholesterol and cholest-8(9)-en-3-beta-ol
CC in the plasma and tissues. {ECO:0000269|PubMed:10391218,
CC ECO:0000269|PubMed:10391219, ECO:0000269|PubMed:10942423,
CC ECO:0000269|PubMed:11493318, ECO:0000269|PubMed:18176751,
CC ECO:0000269|PubMed:25814754}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: MEND syndrome (MEND) [MIM:300960]: An X-linked recessive
CC disorder associated with a defect in sterol biosynthesis. Disease
CC manifestations and severity are highly variable. Clinical features
CC include intellectual disability, short stature, scoliosis, digital
CC abnormalities, cataracts, and dermatologic abnormalities.
CC {ECO:0000269|PubMed:12503101, ECO:0000269|PubMed:20949533,
CC ECO:0000269|PubMed:24459067, ECO:0000269|PubMed:24700572}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- MISCELLANEOUS: Binds to the phenylalkylamine calcium-ion antagonist
CC emopamil, an anti-ischemic drug.
CC -!- SIMILARITY: Belongs to the EBP family. {ECO:0000305}.
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DR EMBL; Z37986; CAA86068.1; -; mRNA.
DR EMBL; CR456815; CAG33096.1; -; mRNA.
DR EMBL; CR542094; CAG46891.1; -; mRNA.
DR EMBL; AF196969; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF196972; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471224; EAW50773.1; -; Genomic_DNA.
DR EMBL; BC001549; AAH01549.1; -; mRNA.
DR EMBL; BC001572; AAH01572.1; -; mRNA.
DR EMBL; BC046501; AAH46501.1; -; mRNA.
DR CCDS; CCDS14300.1; -.
DR PIR; B56122; B56122.
DR RefSeq; NP_006570.1; NM_006579.2.
DR PDB; 6OHT; X-ray; 3.20 A; A/B/C=2-230.
DR PDB; 6OHU; X-ray; 3.53 A; A/B/C=2-230.
DR PDBsum; 6OHT; -.
DR PDBsum; 6OHU; -.
DR AlphaFoldDB; Q15125; -.
DR SMR; Q15125; -.
DR BioGRID; 115921; 244.
DR IntAct; Q15125; 214.
DR STRING; 9606.ENSP00000417052; -.
DR BindingDB; Q15125; -.
DR ChEMBL; CHEMBL4931; -.
DR DrugBank; DB00675; Tamoxifen.
DR DrugCentral; Q15125; -.
DR SwissLipids; SLP:000001209; -.
DR GlyGen; Q15125; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q15125; -.
DR PhosphoSitePlus; Q15125; -.
DR SwissPalm; Q15125; -.
DR BioMuta; EBP; -.
DR DMDM; 17374795; -.
DR EPD; Q15125; -.
DR jPOST; Q15125; -.
DR MassIVE; Q15125; -.
DR MaxQB; Q15125; -.
DR PaxDb; Q15125; -.
DR PeptideAtlas; Q15125; -.
DR PRIDE; Q15125; -.
DR ProteomicsDB; 60452; -.
DR TopDownProteomics; Q15125; -.
DR Antibodypedia; 525; 175 antibodies from 23 providers.
DR DNASU; 10682; -.
DR Ensembl; ENST00000495186.6; ENSP00000417052.1; ENSG00000147155.11.
DR GeneID; 10682; -.
DR KEGG; hsa:10682; -.
DR MANE-Select; ENST00000495186.6; ENSP00000417052.1; NM_006579.3; NP_006570.1.
DR UCSC; uc004djx.5; human.
DR CTD; 10682; -.
DR DisGeNET; 10682; -.
DR GeneCards; EBP; -.
DR GeneReviews; EBP; -.
DR HGNC; HGNC:3133; EBP.
DR HPA; ENSG00000147155; Tissue enhanced (liver).
DR MalaCards; EBP; -.
DR MIM; 300205; gene.
DR MIM; 300960; phenotype.
DR MIM; 302960; phenotype.
DR neXtProt; NX_Q15125; -.
DR OpenTargets; ENSG00000147155; -.
DR Orphanet; 401973; MEND syndrome.
DR Orphanet; 35173; X-linked dominant chondrodysplasia punctata.
DR PharmGKB; PA27587; -.
DR VEuPathDB; HostDB:ENSG00000147155; -.
DR eggNOG; KOG4826; Eukaryota.
DR GeneTree; ENSGT00530000063715; -.
DR HOGENOM; CLU_072128_0_0_1; -.
DR InParanoid; Q15125; -.
DR OMA; FEGYFAY; -.
DR OrthoDB; 1130914at2759; -.
DR PhylomeDB; Q15125; -.
DR TreeFam; TF314716; -.
DR BioCyc; MetaCyc:ENSG00000147155-MON; -.
DR BRENDA; 5.3.3.5; 2681.
DR PathwayCommons; Q15125; -.
DR Reactome; R-HSA-6807047; Cholesterol biosynthesis via desmosterol.
DR Reactome; R-HSA-6807062; Cholesterol biosynthesis via lathosterol.
DR SABIO-RK; Q15125; -.
DR SignaLink; Q15125; -.
DR UniPathway; UPA00063; -.
DR BioGRID-ORCS; 10682; 9 hits in 705 CRISPR screens.
DR ChiTaRS; EBP; human.
DR GenomeRNAi; 10682; -.
DR Pharos; Q15125; Tchem.
DR PRO; PR:Q15125; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q15125; protein.
DR Bgee; ENSG00000147155; Expressed in right lobe of liver and 203 other tissues.
DR ExpressionAtlas; Q15125; baseline and differential.
DR Genevisible; Q15125; HS.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; ISM:GO_Central.
DR GO; GO:0005635; C:nuclear envelope; IDA:UniProtKB.
DR GO; GO:0000247; F:C-8 sterol isomerase activity; ISS:UniProtKB.
DR GO; GO:0047750; F:cholestenol delta-isomerase activity; IEA:UniProtKB-EC.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0004769; F:steroid delta-isomerase activity; IDA:UniProtKB.
DR GO; GO:0006695; P:cholesterol biosynthetic process; IDA:UniProtKB.
DR GO; GO:0033489; P:cholesterol biosynthetic process via desmosterol; TAS:Reactome.
DR GO; GO:0033490; P:cholesterol biosynthetic process via lathosterol; TAS:Reactome.
DR GO; GO:0008203; P:cholesterol metabolic process; IMP:GO_Central.
DR GO; GO:0030097; P:hemopoiesis; IEA:Ensembl.
DR GO; GO:0043931; P:ossification involved in bone maturation; IMP:GO_Central.
DR GO; GO:0016126; P:sterol biosynthetic process; IBA:GO_Central.
DR InterPro; IPR007905; EBP.
DR InterPro; IPR033118; EXPERA.
DR PANTHER; PTHR14207; PTHR14207; 1.
DR PROSITE; PS51751; EXPERA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cataract; Cholesterol biosynthesis;
KW Cholesterol metabolism; Cytoplasmic vesicle; Disease variant; Dwarfism;
KW Endoplasmic reticulum; Ichthyosis; Isomerase; Lipid biosynthesis;
KW Lipid metabolism; Membrane; Nucleus; Reference proteome;
KW Steroid biosynthesis; Steroid metabolism; Sterol biosynthesis;
KW Sterol metabolism; Transmembrane; Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:25944712"
FT CHAIN 2..230
FT /note="3-beta-hydroxysteroid-Delta(8),Delta(7)-isomerase"
FT /id="PRO_0000174342"
FT TRANSMEM 29..49
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 66..86
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 121..141
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 185..205
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 61..204
FT /note="EXPERA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01087"
FT MOD_RES 2
FT /note="N-acetylthreonine"
FT /evidence="ECO:0007744|PubMed:25944712"
FT VARIANT 18
FT /note="L -> P (in MEND; patients have mildly increased
FT concentrations of plasma 8(9)-cholestenol and 8-
FT dehydrocholesterol; probable hypomorphic mutation;
FT dbSNP:rs104894795)"
FT /evidence="ECO:0000269|PubMed:12503101"
FT /id="VAR_074633"
FT VARIANT 47
FT /note="W -> C (in MEND; patients have increased
FT concentrations of plasma 8(9)-cholestenol, 8-
FT dehydrocholesterol and 7-dehydrocholesterol; probable
FT hypomorphic mutation; dbSNP:rs587783599)"
FT /evidence="ECO:0000269|PubMed:20949533"
FT /id="VAR_074634"
FT VARIANT 47
FT /note="W -> R (in MEND; patients have increased
FT concentrations of plasma 8-dehydrocholesterol and 8(9)-
FT cholestenol; probable hypomorphic mutation;
FT dbSNP:rs878854359)"
FT /evidence="ECO:0000269|PubMed:24459067"
FT /id="VAR_074635"
FT VARIANT 75
FT /note="I -> N (in MEND; patients have increased plasma
FT levels of 8(9)-cholestenol; probable hypomorphic mutation;
FT dbSNP:rs797045153)"
FT /evidence="ECO:0000269|PubMed:24700572"
FT /id="VAR_074636"
FT VARIANT 80
FT /note="E -> K (in CDPX2; dbSNP:rs104894800)"
FT /evidence="ECO:0000269|PubMed:10391219"
FT /id="VAR_012105"
FT VARIANT 103
FT /note="E -> K (in CDPX2)"
FT /evidence="ECO:0000269|PubMed:18176751"
FT /id="VAR_074637"
FT VARIANT 110
FT /note="R -> Q (in CDPX2; dbSNP:rs1602090481)"
FT /evidence="ECO:0000269|PubMed:10391218"
FT /id="VAR_012106"
FT VARIANT 147
FT /note="R -> G (in CDPX2)"
FT /evidence="ECO:0000269|PubMed:11493318"
FT /id="VAR_012107"
FT VARIANT 147
FT /note="R -> H (in CDPX2; dbSNP:rs28935174)"
FT /evidence="ECO:0000269|PubMed:10391219,
FT ECO:0000269|PubMed:10942423, ECO:0000269|PubMed:25814754"
FT /id="VAR_012108"
FT MUTAGEN 68
FT /note="W->A: Reduces catalytic activity to less than 35% of
FT wild-type."
FT /evidence="ECO:0000269|PubMed:9894009"
FT MUTAGEN 75
FT /note="I->A: Reduces catalytic activity to less than 35% of
FT wild-type."
FT /evidence="ECO:0000269|PubMed:9894009"
FT MUTAGEN 76
FT /note="H->A: Reduces catalytic activity to less than 10% of
FT wild-type."
FT /evidence="ECO:0000269|PubMed:9894009"
FT MUTAGEN 80
FT /note="E->A: Reduces catalytic activity to less than 10% of
FT wild-type."
FT /evidence="ECO:0000269|PubMed:9894009"
FT MUTAGEN 111
FT /note="Y->W: Reduces catalytic activity to less than 2% of
FT wild-type."
FT /evidence="ECO:0000269|PubMed:12760743"
FT MUTAGEN 121
FT /note="M->A: Reduces catalytic activity to less than 35% of
FT wild-type."
FT /evidence="ECO:0000269|PubMed:12760743"
FT MUTAGEN 121
FT /note="M->V: No effect on catalytic activity."
FT /evidence="ECO:0000269|PubMed:12760743"
FT MUTAGEN 122
FT /note="E->A: Reduces catalytic activity to less than 10% of
FT wild-type."
FT /evidence="ECO:0000269|PubMed:9894009"
FT MUTAGEN 125
FT /note="T->A: Reduces catalytic activity to less than 10% of
FT wild-type."
FT /evidence="ECO:0000269|PubMed:9894009"
FT MUTAGEN 188
FT /note="Y->A: Reduces catalytic activity to less than 35% of
FT wild-type."
FT /evidence="ECO:0000269|PubMed:9894009"
FT MUTAGEN 189
FT /note="F->A: Reduces catalytic activity to less than 35% of
FT wild-type."
FT /evidence="ECO:0000269|PubMed:12760743"
FT MUTAGEN 189
FT /note="F->L: No effect on catalytic activity."
FT /evidence="ECO:0000269|PubMed:12760743"
FT MUTAGEN 193
FT /note="N->A: Reduces catalytic activity to less than 10% of
FT wild-type."
FT /evidence="ECO:0000269|PubMed:9894009"
FT MUTAGEN 196
FT /note="W->A: Reduces catalytic activity to less than 10% of
FT wild-type."
FT /evidence="ECO:0000269|PubMed:9894009"
FT CONFLICT 187..188
FT /note="FY -> IF (in Ref. 2; CAG33096)"
FT /evidence="ECO:0000305"
FT HELIX 28..51
FT /evidence="ECO:0007829|PDB:6OHT"
FT HELIX 61..85
FT /evidence="ECO:0007829|PDB:6OHT"
FT STRAND 86..88
FT /evidence="ECO:0007829|PDB:6OHT"
FT HELIX 96..106
FT /evidence="ECO:0007829|PDB:6OHT"
FT STRAND 107..109
FT /evidence="ECO:0007829|PDB:6OHT"
FT TURN 111..114
FT /evidence="ECO:0007829|PDB:6OHT"
FT HELIX 116..127
FT /evidence="ECO:0007829|PDB:6OHT"
FT HELIX 129..139
FT /evidence="ECO:0007829|PDB:6OHT"
FT TURN 140..143
FT /evidence="ECO:0007829|PDB:6OHT"
FT HELIX 146..171
FT /evidence="ECO:0007829|PDB:6OHT"
FT TURN 172..174
FT /evidence="ECO:0007829|PDB:6OHT"
FT HELIX 182..189
FT /evidence="ECO:0007829|PDB:6OHT"
FT HELIX 190..215
FT /evidence="ECO:0007829|PDB:6OHT"
SQ SEQUENCE 230 AA; 26353 MW; 3931A9DE3DBAFA04 CRC64;
MTTNAGPLHP YWPQHLRLDN FVPNDRPTWH ILAGLFSVTG VLVVTTWLLS GRAAVVPLGT
WRRLSLCWFA VCGFIHLVIE GWFVLYYEDL LGDQAFLSQL WKEYAKGDSR YILGDNFTVC
METITACLWG PLSLWVVIAF LRQHPLRFIL QLVVSVGQIY GDVLYFLTEH RDGFQHGELG
HPLYFWFYFV FMNALWLVLP GVLVLDAVKH LTHAQSTLDA KATKAKSKKN
